Purification and properties of serine protease from Halobacterium halobium.
Pure extracellular serine protease was isolated from the culture filtrate of Halobacterium halobium by bacitracin-Sepharose affinity chromatography. The enzyme activity was completely and irreversibly lost if the NaCl concentration fell below 2 M. The protease consists of one polypeptide chain with...
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| 出版年: | J Bacteriol |
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| 主要な著者: | , , , , , , , |
| フォーマット: | Artigo |
| 言語: | Inglês |
| 出版事項: |
American Society for Microbiology (ASM)
1983
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| 主題: | |
| オンライン･アクセス: | https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC217755/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/6348027/ https://ncbi.nlm.nih.govhttps://doi.org/10.1128/jb.155.2.826-830.1983 |
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